SUMOylation processes themselves can be controlled by SUMOylation (reviewed in Wilkinson and Henley 2010). The SUMO E3 ligases PIAS4, RANBP2, and TOPORS are SUMOylated, as is the single SUMO E2 enzyme, UBE2I (UBC9). SUMOylation affects the subcellular location of PIAS4 and TOPORS and affects the activity of PIAS4 and UBE2I.
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PIAS4 is SUMOylated at lysine-35 with SUMO1 (Ihara et al. 2005). SUMOylation of PIAS4 at lysine-35 decreases its localization with PML. SUMOylated PIAS4 is able to increase SUMOylation and transcriptional activity of TCF4.
UBE2I (UBC9) is SUMOylated at lysine-14 with SUMO1 (Knipscheer et al. 2008). SUMOylation alters the target specificity of UBE2I, decreasing its SUMOylation activity towards RanGAP1 and increasing it towards SP100.
RANBP2 SUMOylates RANBP2 at lysine-2592, lysine-2650, and lysine-2723 with SUMO1 (Pichler et al. 2002, Pichler et al. 2004, Cooper et al. 2005). RANBP2 does not resemble HECT or RING type SUMO E3 ligases and instead uses hydrophobic interactions with UBE2I (UBC9) to catalyze SUMOylation.
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